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3f8u
From Proteopedia
| 3f8u, resolution 2.60Å () | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Sites: | and | ||||||||
| Ligands: | |||||||||
| Gene: | PDIA3, ERP57, ERP60, GRP58 (Homo sapiens), TAPBP, NGS17, TAPA (Homo sapiens) | ||||||||
| Activity: | Protein disulfide-isomerase, with EC number 5.3.4.1 | ||||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
Tapasin/ERp57 heterodimer
Tapasin is a glycoprotein critical for loading major histocompatibility complex (MHC) class I molecules with high-affinity peptides. It functions within the multimeric peptide-loading complex (PLC) as a disulfide-linked, stable heterodimer with the thiol oxidoreductase ERp57, and this covalent interaction is required to support optimal PLC activity. Here, we present the 2.6 A resolution structure of the tapasin-ERp57 core of the PLC. The structure revealed that tapasin interacts with both ERp57 catalytic domains, accounting for the stability of the heterodimer, and provided an example of a protein disulfide isomerase family member interacting with substrate. Mutational analysis identified a conserved surface on tapasin that interacted with MHC class I molecules and was critical for peptide loading and editing functions of the tapasin-ERp57 heterodimer. By combining the tapasin-ERp57 structure with those of other defined PLC components, we present a molecular model that illuminates the processes involved in MHC class I peptide loading.
Insights into MHC Class I Peptide Loading from the Structure of the Tapasin-ERp57 Thiol Oxidoreductase Heterodimer., Dong G, Wearsch PA, Peaper DR, Cresswell P, Reinisch KM, Immunity. 2008 Dec 30. PMID:19119025
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
3F8U is a 4 chains structure with sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
- Dong G, Wearsch PA, Peaper DR, Cresswell P, Reinisch KM. Insights into MHC Class I Peptide Loading from the Structure of the Tapasin-ERp57 Thiol Oxidoreductase Heterodimer. Immunity. 2008 Dec 30. PMID:19119025 doi:S1074-7613(08)00544-X
Page seeded by OCA on Wed Sep 22 11:30:05 2010
Categories: Homo sapiens | Protein disulfide-isomerase | Dong, G. | Reinisch, K M. | Alternative splicing | Beta barrel | Endoplasmic reticulum | Glycoprotein | Ig-like domain | Immune system/isomerase complex | Immunoglobulin domain | Isomerase | Membrane | Microsome | Polymorphism | Protein disulfide isomerase | Redox-active cente | Thioredoxin-like fold
